Exploiting differential dissociation chemistries of O-linked glycopeptide ions for the localization of mucin-type protein glycosylation.

@article{Seipert2009ExploitingDD,
  title={Exploiting differential dissociation chemistries of O-linked glycopeptide ions for the localization of mucin-type protein glycosylation.},
  author={Richard R. Seipert and Eric D. Dodds and Carlito B. Lebrilla},
  journal={Journal of proteome research},
  year={2009},
  volume={8 2},
  pages={493-501}
}
From a glycoproteomic perspective, the unambiguous localization of O-linked oligosaccharide attachment sites is fraught with analytical obstacles. Because no consensus protein sequence exists for O-glycosylation, there is potential for glycan attachment at numerous serine and threonine residues of a given protein. The well-established tendency for O-glycan attachment to occur within serine and threonine rich domains adds further complication to site-specific assignment of mucin-type… CONTINUE READING